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A cytokinin-binding protein complex from tobacco leaves

The 57 kDa subunit has high homology to S-adenosyl-L-homocysteine hydrolase

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Abstract

A cytokinin binding protein complex (CBP130) has been purified from tobacco leaves (Nicotiana sylvestris). It contains two protein species of 57 and 36 kDa (CBP57 and CBP36). The cDNAs encoding CBP57 have been isolated from a tobacco cDNA library. Their predicted amino acid sequences showed significant homology between CBP57 and S-adenosyl-L-homocysteine (SAH) hydrolase, which catalyzes the reversible hydrolysis of SAH, a methyltransferase inhibitor. A combination of gel filtration an western blot analysis revealed that both CBP57 and benzyladenine (BA)-binding activity were eluted at a peak of 130 kDa. A purified CBP130 fraction contains SAH hydrolase activity. We discuss possible CBP57 as a cytokinin receptor subunit and its possible role as a regulator of methylation.

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Authors and Affiliations

  1. Center for Gene Research, Nagoya University, 464-01, Nagoya, Japan

    Shinichi Mitsui, Tatsuya Wakasugi & Masahiro Sugiura

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  1. Shinichi Mitsui
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  2. Tatsuya Wakasugi
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  3. Masahiro Sugiura
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Mitsui, S., Wakasugi, T. & Sugiura, M. A cytokinin-binding protein complex from tobacco leaves. Plant Growth Regul 18, 39–43 (1996). https://doi.org/10.1007/BF00028486

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